SYL_BIFLO
ID SYL_BIFLO Reviewed; 987 AA.
AC Q8G4D8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=BL1450;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AE014295; AAN25245.1; -; Genomic_DNA.
DR RefSeq; NP_696609.1; NC_004307.2.
DR RefSeq; WP_011068058.1; NC_004307.2.
DR AlphaFoldDB; Q8G4D8; -.
DR SMR; Q8G4D8; -.
DR STRING; 206672.BL1450; -.
DR EnsemblBacteria; AAN25245; AAN25245; BL1450.
DR KEGG; blo:BL1450; -.
DR PATRIC; fig|206672.9.peg.308; -.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q8G4D8; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 3.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..987
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151978"
FT MOTIF 69..80
FT /note="'HIGH' region"
FT MOTIF 760..764
FT /note="'KMSKS' region"
FT BINDING 763
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 987 AA; 110295 MW; A5EADD58993F6EA8 CRC64;
MSDNEKSTQT EEPNFRYNAA LAQDIENKWQ KIWDEQGTFW AANVNGDLKD GKGRNAEGRT
AYFAMDMFPY PSGKGLHVGH PLGYLASDVV SRYHRMKGEN VLHAMGYDAF GLPAEQYAVQ
TGQHPRVTTE ANIANMSRQL HRMGLSFDNR RTFATIDPGY VRWTQWIFSR IYDSWYDEDA
TNPSGSKGSA RPIAELVAKF ESGEKAIPGH ESDGKQWSDL TDAEQQDILN DFRLAYISKS
PVNWCPGLGT VLANEEVTAE GKSERGNFPV FQRELRQWSM RITKYGHRLI ADLDGINWPE
KVKLMQRNWI GESHGASVHF IVATADGDKD MEIYTTRPDT LFGTTFAVVS PEHHLLENVP
AEWPADVPED WKGGYANPVE AVKAYRLAAE AKTAKDRVNE AGEKTGLFTG LYATNPITGA
KLPLFTADYV LMDYGTGAIM AVPGGDQRDY DFAVKFGLPV IYTVTPLPDS GDDLANYEGK
APFVSHDGIV INSSVEATEA KGDALSLNGL RVDDAIAKVN AWLESAGVGK GTVSYRLRDW
LFSRQRYWGE PFPIVYGEDG TPHLLPDSAL PINLPDVPDY EPRTFDPMDA ESNPEAPLSR
NEDWVKVELD LGDGKKTYYR DTNTMPNWAG SCWYYMRYID PTDTKHMVEK DEFDYWMGPN
HNKYSGDEGG VDLYIGGVEH AVLHLLYSRF WHKVLFDLGY VDSAEPFHKL FNQGMIQAYA
YTDDRGQYVP ADEVVEGPAD ASGEPTFTWN GEHANREFGK MGKSLKNIVT PDYMYENYGA
DTFRLYEMSM GPLDESRPWN TRNVVGGMRF LQRLWRNVVD ETTGQAHVTE DTPDEKTLKL
LNNTIAEVTA EMEGMRPNTA IAKLIVLNNH LTGLKAVPRA AVEPLILMLA PIAPHICEEM
WSKLGHAESL SAEPWPVADE RYVGHDTVTA VVQIKGKVRA KLEVPVDIDP ADLEKQALAA
VADRLGGKEP RKVIVKAPKI VSIVPAE
